RIGIN, ANOTHER PHAGOCYTOSIS‐STIMULATING TETRAPEPTIDE ISOLATED FROM HUMAN IgG: Confirmations of a Hypothesis
N. Veretennikova, G. I. Chipens, Gregory V. Nikiforovich, YA. R. BETINSH
Abstract
N. Veretennikova, G. I. Chipens, Gregory V. Nikiforovich, YA. R. BETINSH
Abstract
Structure-function and conformational studies of the molecule of phagocytosis-stimulating tetrapeptide tuftsin permitted the conclusion that among products resulting from splitting of H-chain of IgG Human EU by trypsin, besides tuftsin (sequence 289-292), tuftsin-like tetrapeptide Gly-Gln-Pro-Arg may be also present; theoretical conformational analysis shows a considerable similarity of spatial arrangement of this tetrapeptide and tuftsin which testifies in favour of potential tuftsin-like activity of the tetrapeptide. Gly-Gln-Pro-Arg was synthesized and its phagocytosis stimulating activity was found equal to that of tuftsin.
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Structure-function and conformational studies of the molecule of phagocytosis-stimulating tetrapeptide tuftsin permitted the conclusion that among products resulting from splitting of H-chain of IgG Human EU by trypsin, besides tuftsin (sequence 289-292), tuftsin-like tetrapeptide Gly-Gln-Pro-Arg may be also present; theoretical conformational analysis shows a considerable similarity of spatial arrangement of this tetrapeptide and tuftsin which testifies in favour of potential tuftsin-like activity of the tetrapeptide. Gly-Gln-Pro-Arg was synthesized and its phagocytosis stimulating activity was found equal to that of tuftsin.
Key concepts: Tuftsin, Tetrapeptide, Phagocytosis, Trypsin, Chemistry, Peptide, Stereochemistry, Biochemistry